ID   CSKMT_DANRE             Reviewed;         254 AA.
AC   Q501S4;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Citrate synthase-lysine N-methyltransferase CSKMT, mitochondrial {ECO:0000250|UniProtKB:A8MUP2};
DE            Short=CS-KMT {ECO:0000250|UniProtKB:A8MUP2};
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:A8MUP2};
DE   AltName: Full=Methyltransferase-like protein 12, mitochondrial {ECO:0000250|UniProtKB:A8MUP2};
DE   Flags: Precursor;
GN   Name=cskmt {ECO:0000250|UniProtKB:A8MUP2};
GN   Synonyms=mettl12 {ECO:0000250|UniProtKB:A8MUP2}; ORFNames=zgc:113305;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protein-lysine methyltransferase that selectively
CC       trimethylates citrate synthase (CS) in mitochondria. Seems to conduct
CC       trimethylation in a highly distributive manner rather than in a
CC       processive manner, and thus introduces a single methyl group per
CC       binding event. {ECO:0000250|UniProtKB:A8MUP2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[citrate synthase] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[citrate synthase] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:55544, Rhea:RHEA-COMP:14212, Rhea:RHEA-COMP:14213,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC         Evidence={ECO:0000250|UniProtKB:A8MUP2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-methyl-L-lysyl-[citrate synthase] + S-adenosyl-L-
CC         methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl-[citrate synthase] +
CC         S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:55548, Rhea:RHEA-
CC         COMP:14213, Rhea:RHEA-COMP:14214, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929,
CC         ChEBI:CHEBI:61976; Evidence={ECO:0000250|UniProtKB:A8MUP2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6),N(6)-dimethyl-L-lysyl-[citrate synthase] + S-adenosyl-L-
CC         methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[citrate
CC         synthase] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:55552,
CC         Rhea:RHEA-COMP:14214, Rhea:RHEA-COMP:14215, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961,
CC         ChEBI:CHEBI:61976; Evidence={ECO:0000250|UniProtKB:A8MUP2};
CC   -!- ACTIVITY REGULATION: Citrate synthase-lysine methyltransferase activity
CC       is inhibited by S-adenosylhomocysteine (AdoHcy) and oxaloacetate (OAA).
CC       {ECO:0000250|UniProtKB:A8MUP2}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:A8MUP2}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH95893.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC095893; AAH95893.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001018613.1; NM_001020777.1.
DR   AlphaFoldDB; Q501S4; -.
DR   SMR; Q501S4; -.
DR   STRING; 7955.ENSDARP00000071604; -.
DR   PaxDb; Q501S4; -.
DR   DNASU; 553815; -.
DR   GeneID; 553815; -.
DR   KEGG; dre:553815; -.
DR   CTD; 751071; -.
DR   ZFIN; ZDB-GENE-050522-31; cskmt.
DR   eggNOG; KOG2352; Eukaryota.
DR   InParanoid; Q501S4; -.
DR   PhylomeDB; Q501S4; -.
DR   PRO; PR:Q501S4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0016278; F:lysine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0018027; P:peptidyl-lysine dimethylation; ISS:UniProtKB.
DR   GO; GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB.
DR   GO; GO:0018023; P:peptidyl-lysine trimethylation; ISS:UniProtKB.
DR   GO; GO:0006479; P:protein methylation; ISS:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR025714; Methyltranfer_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF13847; Methyltransf_31; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; Mitochondrion; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; Transit peptide.
FT   TRANSIT         1..45
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           46..254
FT                   /note="Citrate synthase-lysine N-methyltransferase CSKMT,
FT                   mitochondrial"
FT                   /id="PRO_0000349201"
SQ   SEQUENCE   254 AA;  28331 MW;  E22C6C5BB490D61A CRC64;
     MLLNRFLVPL RSLQKLTQAR RWHQTSLIND LVVNMDKKAM WDRFYTENGS KGQFKNFEWF
     FGFPSVKDLV LPALQAMSCS HSGPLHILDM GCGTSALGPC IYSTSPCAVR VTCADISPVA
     VKLMEEHTKS TSTQPCNPSS ALVFLELDCT QMTGHFKSRS LDLILDKGTT DALVRSKEGQ
     VKAGQILRQS LQVLRPSGSF LQFSDEDPDA RLIWLEREVQ GAEVTADVGV QEIGELRGVS
     YFCYQISPRS RPHS